Michael L. Johnson, Jo M. Holt, Gary K. Ackers's Biothermodynamics, Part B PDF

By Michael L. Johnson, Jo M. Holt, Gary K. Ackers

ISBN-10: 0123747767

ISBN-13: 9780123747761

Using thermodynamics in organic examine may be equated to an power book-keeping process. whereas the constitution and serve as of a molecule is critical, it's both vital to understand what drives the strength strength. those tools glance to respond to: What are the assets of strength that force the functionality? Which of the pathways are of organic value? because the base of macromolecular buildings maintains to extend via robust suggestions of molecular biology, corresponding to X-ray crystal info and spectroscopy equipment, the significance of established and trustworthy equipment for answering those questions will proceed to extend in addition. This quantity provides refined tools for estimating the thermodynamic parameters of particular protein-protein, protein-DNA and small molecule interactions.* Elucidates the relationships among constitution and energetics and their purposes to molecular layout, helping researchers within the layout of medically very important molecules * offers a "must-have" tools quantity that retains MIE dealers and on-line subscribers updated with the most recent study * bargains step by step lab directions, together with invaluable apparatus, from an international study neighborhood

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Extra resources for Biothermodynamics, Part B

Example text

Miklos, A. , Schlesinger, A. , Slade, K. , and Zigoneanu, I. G. (2008). Protein NMR under physiological conditions. Biochemistry 48, 226–234. Privalov, P. , and Khechinashvili, N. N. (1974). A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J. Mol. Biol. 86, 665–684. Qu, Y. , and Bolen, D. W. (2003). Hydrogen exchange kinetics of RNase A and the urea: TMAO paradigm. Biochemistry 42, 5837–5849. Richards, F. M. (1977). Areas, volumes, packing, and protein structure.

And Kallen, R. G. (1972). Primary structure effects on peptide group hydrogen exchange. Biochemistry 11, 150–158. Molyneux, P. (1983). Water-soluble synthetic polymers: Properties and behavior. CRC Press, Boca Raton, CA. Munishkina, L. , Fink, A. , and Uversky, V. N. (2008). Guiding protein aggregation with macromolecular crowding. Biochemistry 47, 8993–9006. Neira, J. , Itzhaki, L. , Otzen, D. , and Fersht, A. R. (1997). Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis. J.

A 300-g/L exchange sample will contain impurities at weight concentrations rivaling that of the test protein. Expense is a factor for the crowding agent because tens to hundreds of grams are necessary for characterization and to perform detailed exchange studies. Many polydisperse polymers satisfy these requirements. Polydisperse crowders include synthetic polymers, and naturally occurring polymers such as polysaccharides. One advantage of choosing synthetic polymers is that they are often available in a range of molecular weights.

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Biothermodynamics, Part B by Michael L. Johnson, Jo M. Holt, Gary K. Ackers

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